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• W3195304920 abstract "Amyloidosis is a term referring to a group of various protein-misfolding diseases wherein normally soluble proteins form aggregates as insoluble amyloid fibrils. How, or whether, amyloid fibrils contribute to tissue damage in amyloidosis has been the topic of debate. In vitro studies have demonstrated the appearance of small globular oligomeric species during the incubation of amyloid beta peptide (Aβ). Nerve biopsy specimens from patients with systemic amyloidosis have suggested that globular structures similar to Aβ oligomers were generated from amorphous electron-dense materials and later developed into mature amyloid fibrils. Schwann cells adjacent to amyloid fibrils become atrophic and degenerative, suggesting that the direct tissue damage induced by amyloid fibrils plays an important role in systemic amyloidosis. In contrast, there is increasing evidence that oligomers, rather than amyloid fibrils, are responsible for cell death in neurodegenerative diseases, particularly Alzheimer’s disease. Disease-modifying therapies based on the pathophysiology of amyloidosis have now become available. Aducanumab, a human monoclonal antibody against the aggregated form of Aβ, was recently approved for Alzheimer’s disease, and other monoclonal antibodies, including gantenerumab, solanezumab, and lecanemab, could also be up for approval. As many other agents for amyloidosis will be developed in the future, studies to develop sensitive clinical scales for identifying improvement and markers that can act as surrogates for clinical scales should be conducted." @default.
• W3195304920 created "2021-08-30" @default.
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• W3195304920 date "2021-08-22" @default.
• W3195304920 modified "2023-09-27" @default.
• W3195304920 title "Significance of Oligomeric and Fibrillar Species in Amyloidosis: Insights into Pathophysiology and Treatment" @default.
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• W3195304920 doi "https://doi.org/10.3390/molecules26165091" @default.
• W3195304920 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8401015" @default.
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• W3195304920 hasPublicationYear "2021" @default.
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